Cloning, sequencing and expression of vat, a cdc48/p97 atpase homologue from 
the archaeon thermoplasma acidophilum

Pamnani, V.; Tamura, T.; Lupas, A.; Peters, J.; Cejka, Z.; Ashraf, W.; Baumeister, W.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Cloning, sequencing and expression of vat, a cdc48/p97 atpase homologue from the archaeon thermoplasma acidophilum

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Pamnani, V., Tamura, T., Lupas, A., Peters, J., Cejka, Z., Ashraf, W., et al. (1997). Cloning, sequencing and expression of vat, a cdc48/p97 atpase homologue from the archaeon thermoplasma acidophilum. FEBS Letters, 404(2-3), 263-268.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-729E-9

Abstract

A member of the AAA family of Mg2+-ATPases from the archaeon Thermoplasma acidophilum has been cloned and expressed in Escherichia coli. The protein, VCP-like ATPase of Thermoplasma acidophilum (VAT), is a homologue of SAV from Sulfolobus acidocaldarius and CdcH of Halobacterium salinarium, and belongs to the CDC48/VCP/p97 subfamily. The deduced product of the vat gene is 745 residues long (M(r) 83 000), which has an optimal Mg2+-ATPase activity at 70 degrees C. Electron microscopy shows the purified protein to form single and double homo-hexameric rings, Although the symmetry is different, the appearance of the complexes formed of two rings resembles the 20S proteasome and Hsp60/GroEL. (C) 1997 Federation of European Biochemical Societies. [References: 42]